Prion variant maintained only at high levels of the Hsp104 disaggregase

@article{Borchsenius2005PrionVM,
  title={Prion variant maintained only at high levels of the Hsp104 disaggregase},
  author={Andrey S. Borchsenius and Susanne M{\"u}ller and Gary P. Newnam and Sergey G. Inge-Vechtomov and Yury O Chernoff},
  journal={Current Genetics},
  year={2005},
  volume={49},
  pages={21-29}
}
The yeast prion [PSI + ] is a self-perpetuating aggregated isoform of the translation termination factor Sup35. [PSI + ] propagation is promoted by moderate levels and antagonized by high levels of the chaperone Hsp104. In agreement with the model postulating that excess Hsp104 acts on [PSI + ] by disaggregating prion polymers, we show that an increase in Sup35 levels, accompanied by an increase in size of prion aggregates, also partially protects [PSI + ] from elimination by excess Hsp104… CONTINUE READING
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